Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P03300 (POLG_POL1M)

Entry version 211 (13 Nov 2019)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 1 (strain Mahoney)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host epithelial cells. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. Tyrosine kinases are probably involved in the entry process. Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins. Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.4 Publications
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.3 Publications
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP1. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.4 Publications
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytopflasm. After genome has been released, the channel shrinks.1 Publication
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.2 Publications
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153. Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (PubMed:24390337). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (PubMed:24390337).3 Publications
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.1 Publication
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.3 Publications
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.1 Publication
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (PubMed:15914217, PubMed:17079330). Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (Probable).1 Publication2 Publications
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed 'unlinkase'. VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.5 Publications
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity.1 Publication
Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein (PubMed:8097606). Cleaves also host PABPC1 and contributes to host translation shutoff (PubMed:18632855). Protease 3C: Cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production (PubMed:24390337).3 Publications
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.1 Publication

Caution

Protein 3A: Has been proposed to interact with host LIS1/NUF (PubMed:16138011), but this has not been confirmed by other studies (PubMed:21345960).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. EC:3.4.22.29
  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation EC:3.4.22.28

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei25Involved in the interaction with human RTN3By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei901For Protease 2A activityBy similarity1
Active sitei919For Protease 2A activityBy similarity1
Active sitei990For Protease 2A activityBy similarity1
Active sitei1605For protease 3C activityPROSITE-ProRule annotation1
Active sitei1636For protease 3C activityPROSITE-ProRule annotation1
Active sitei1712For protease 3C activityPROSITE-ProRule annotation1
Active sitei2076For RdRp activity1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1256 – 1263ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host MDA5 by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

Protein family/group databases

MEROPS protease database

More...MEROPSi		C03.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
P1
Capsid protein VP0
Alternative name(s):
VP4-VP2
Capsid protein VP4
Alternative name(s):
P1A
Virion protein 4
Capsid protein VP2
Alternative name(s):
P1B
Virion protein 2
Capsid protein VP3
Alternative name(s):
P1C
Virion protein 3
Capsid protein VP1
Alternative name(s):
P1D
Virion protein 1
P2
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.151 Publication)
Short name:
P2C
P3
Protein 3AB
Protein 3A
Short name:
P3A
Viral protein genome-linked
Short name:
VPg
Alternative name(s):
Protein 3B
Short name:
P3B
Protein 3CD (EC:3.4.22.28)
Protease 3C (EC:3.4.22.28)
Short name:
P3C
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPoliovirus type 1 (strain Mahoney)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri12081 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Picornavirales › Picornaviridae › Enterovirus › Enterovirus C ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000356 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000149468 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Capsid protein VP0 :
Capsid protein VP4 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Viral protein genome-linked :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 1520CytoplasmicSequence analysisAdd BLAST1519
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1521 – 1536Sequence analysisAdd BLAST16
Topological domaini1537 – 2209CytoplasmicSequence analysisAdd BLAST673

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2G → A: 100% loss of myristoylation. Impaired viral assembly. 1 Publication1
Mutagenesisi3A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. 1 Publication1
Mutagenesisi3A → G, L or V: No effect on myristoylation and virus growth. 1 Publication1
Mutagenesisi3A → H: No effect on myristoylation. Severe reduction in specific infectivity. 1 Publication1
Mutagenesisi264H → G: Complete loss of VP0 cleavage. 1 Publication1
Mutagenesisi264H → T: Complete loss of VP0 cleavage. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5127

Drug and drug target database

More...DrugBanki		DB08014 (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE
DB08012 (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE
DB08013 (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE
DB04137 Guanosine-5'-Triphosphate
DB08231 Myristic acid
DB03963 S-(Dimethylarsenic)Cysteine
DB03203 Sphingosine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004246862 – 2209Genome polyproteinAdd BLAST2208
ChainiPRO_00004246872 – 881P1Add BLAST880
ChainiPRO_00004246882 – 341Capsid protein VP0Sequence analysisAdd BLAST340
ChainiPRO_00000400802 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000004008170 – 341Capsid protein VP2Sequence analysisAdd BLAST272
ChainiPRO_0000040082342 – 579Capsid protein VP3Sequence analysisAdd BLAST238
ChainiPRO_0000040083580 – 881Capsid protein VP1Sequence analysisAdd BLAST302
ChainiPRO_0000424689882 – 1456P2Add BLAST575
ChainiPRO_0000040084882 – 1030Protease 2ASequence analysisAdd BLAST149
ChainiPRO_00000400851031 – 1127Protein 2BSequence analysisAdd BLAST97
ChainiPRO_00000400861128 – 1456Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004246901457 – 2209P3Add BLAST753
ChainiPRO_00004246911457 – 1565Protein 3ABSequence analysisAdd BLAST109
ChainiPRO_00004246921457 – 1543Protein 3ASequence analysisAdd BLAST87
ChainiPRO_00000400881544 – 1565Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004246931566 – 2209Protein 3CDSequence analysisAdd BLAST644
ChainiPRO_00000400891566 – 1747Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00000400901748 – 2209RNA-directed RNA polymeraseAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by host3 Publications1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1546O-(5'-phospho-RNA)-tyrosine1 Publication1
Modified residuei1546O-UMP-tyrosine; transient2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion.2 Publications
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.1 Publication
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion.1 Publication
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei341 – 342Cleavage; by Protease 3CSequence analysis2
Sitei881 – 882Cleavage; by Protease 2ASequence analysis2
Sitei1030 – 1031Cleavage; by Protease 3CSequence analysis2
Sitei1127 – 1128Cleavage; by Protease 3CSequence analysis2
Sitei1456 – 1457Cleavage; by Protease 3CSequence analysis2
Sitei1543 – 1544Cleavage; by Protease 3CSequence analysis2
Sitei1565 – 1566Cleavage; by Protease 3CSequence analysis2
Sitei1748 – 1749Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P03300

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P03300

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein VP1:

Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid.

Interacts with human PVR.

Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP0:

Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2:

Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid. Capsid protein VP3:

Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid.

Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP4:

Interacts with capsid protein VP1 and capsid protein VP3. Protein 2C:

Interacts with cellular Vimentin/VIM and BECN1; these interactions play important roles in the viral replication (By similarity). Protein 2C:

Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis. Protein 2C:

Interacts with host BECN1 and DHX9 and possibly presents a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases. Protein 2C: N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Protein 3AB:

Interacts with protein 3CD. Protein 3A: Homodimerizes and interacts with host GBF1. Protein 3A:

Interacts with host ACBD3 (PubMed:22258260). Viral protein genome-linked:

Interacts with RNA-directed RNA polymerase. Protein 3CD:

Interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase:

Interacts with Viral protein genome-linked and with protein 3CD.

By similarity8 Publications

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P03300

Protein interaction database and analysis system

More...IntActi		P03300, 4 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P03300

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12209
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P03300

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P03300

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1232 – 1388SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1566 – 1744Peptidase C3PROSITE-ProRule annotationAdd BLAST179
Domaini1975 – 2090RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni580 – 600Amphipatic alpha-helixSequence analysisAdd BLAST21
Regioni1457 – 1479DisorderedAdd BLAST23

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...CDDi		cd00205 rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.870, 1 hit
2.60.120.20, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR014838 P3A
IPR036203 P3A_soluble_dom
IPR000081 Peptidase_C3
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR003138 Pico_P1A
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08727 P3A, 1 hit
PF00548 Peptidase_C3, 1 hit
PF02226 Pico_P1A, 1 hit
PF00947 Pico_P2A, 1 hit
PF01552 Pico_P2B, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 3 hits
PF00910 RNA_helicase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 1 hit
SSF89043 SSF89043, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P03300-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP 
        60         70         80         90        100
SKFTEPIKDV LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS 
       110        120        130        140        150
VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK 
       160        170        180        190        200
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC 
       210        220        230        240        250
LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA RRFCPVDYLL 
       260        270        280        290        300
GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI 
       310        320        330        340        350
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG 
       360        370        380        390        400
SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA 
       410        420        430        440        450
TKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH 
       460        470        480        490        500
WAGSLKFTFL FCGFMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG 
       510        520        530        540        550
LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD 
       560        570        580        590        600
ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA 
       610        620        630        640        650
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS 
       660        670        680        690        700
RSESSIESFF ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK 
       710        720        730        740        750
LEFFTYSRFD MELTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD 
       760        770        780        790        800
DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS 
       810        820        830        840        850
AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP 
       860        870        880        890        900
RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY 
       910        920        930        940        950
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK 
       960        970        980        990       1000
YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV 
      1010       1020       1030       1040       1050
IGIITAGGEG LVAFSDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ 
      1060       1070       1080       1090       1100
ISDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL 
      1110       1120       1130       1140       1150
LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN AAKGLEWVSN 
      1160       1170       1180       1190       1200
KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ 
      1210       1220       1230       1240       1250
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV 
      1260       1270       1280       1290       1300
CLLVHGSPGT GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV 
      1310       1320       1330       1340       1350
IMDDLNQNPD GADMKLFCQM VSTVEFIPPM ASLEEKGILF TSNYVLASTN 
      1360       1370       1380       1390       1400
SSRISPPTVA HSDALARRFA FDMDIQVMNE YSRDGKLNMA MATEMCKNCH 
      1410       1420       1430       1440       1450
QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE RNRRSNIGNC 
      1460       1470       1480       1490       1500
MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV 
      1510       1520       1530       1540       1550
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP 
      1560       1570       1580       1590       1600
NKKPNVPTIR TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA 
      1610       1620       1630       1640       1650
ILPTHASPGE SIVIDGKEVE ILDAKALEDQ AGTNLEITII TLKRNEKFRD 
      1660       1670       1680       1690       1700
IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP VGAVTEQGYL NLGGRQTART 
      1710       1720       1730       1740       1750
LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK RSYFTQSQGE 
      1760       1770       1780       1790       1800
IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT 
      1810       1820       1830       1840       1850
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY 
      1860       1870       1880       1890       1900
GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL 
      1910       1920       1930       1940       1950
PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP 
      1960       1970       1980       1990       2000
GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALKMV 
      2010       2020       2030       2040       2050
LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN 
      2060       2070       2080       2090       2100
LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL 
      2110       2120       2130       2140       2150
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR 
      2160       2170       2180       2190       2200
WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST 

LYRRWLDSF
Length:2,209
Mass (Da):246,540
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF1754F87F2E97D6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti242 – 264RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446 (PubMed:6272282).CuratedAdd BLAST23
Sequence conflicti287I → L in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti309A → V in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti420 – 422DDP → AAS in CAA24446 (PubMed:6272282).Curated3
Sequence conflicti464F → S in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti515T → S in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti855 – 856AV → QL in CAA24446 (PubMed:6272282).Curated2
Sequence conflicti972A → V in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti985A → E in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1140 – 1141NA → QR in CAA24446 (PubMed:6272282).Curated2
Sequence conflicti1619V → A in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1626 – 1627AL → VF in CAA24446 (PubMed:6272282).Curated2
Sequence conflicti1635L → F in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1682G → R in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1722 – 1730VIGMHVGGN → SSGCMLVD in CAA24446 (PubMed:6272282).Curated9
Sequence conflicti1743Y → L in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1752Q → P in CAA24446 (PubMed:6272282).Curated1
Sequence conflicti1759 – 1760EV → DA in CAA24446 (PubMed:6272282).Curated2
Sequence conflicti1840T → I in CAA24446 (PubMed:6272282).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
V01149 Genomic RNA Translation: CAA24461.1
V01148 Genomic RNA Translation: CAA24446.1

Protein sequence database of the Protein Information Resource

More...PIRi		A03898 GNNY2P
A93258 GNNY1P

NCBI Reference Sequences

More...RefSeqi		NP_041277.1, NC_002058.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		919920

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:919920

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral empty capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with R78206

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure of 135S cell entry intermediate

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01149 Genomic RNA Translation: CAA24461.1
V01148 Genomic RNA Translation: CAA24446.1
PIRiA03898 GNNY2P
A93258 GNNY1P
RefSeqiNP_041277.1, NC_002058.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AL2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR6X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR7X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR8X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR9X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1ASJX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1DGIelectron microscopy22.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
1FPTX-ray3.00P665-682[»]
1HXSX-ray2.201580-881[»]
270-341[»]
3342-578[»]
42-69[»]
1L1NX-ray2.10A/B1566-1748[»]
1NG7NMR-A/B1457-1515[»]
1NN8electron microscopy15.001580-881[»]
270-341[»]
3342-576[»]
42-69[»]
1PO1X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1PO2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1POVX-ray2.8002-341[»]
1580-881[»]
3342-579[»]
1RA6X-ray2.00A1749-2209[»]
1RA7X-ray2.35A1749-2209[»]
1RAJX-ray2.50A1817-2209[»]
1RDRX-ray2.40A1749-2209[»]
1TQLX-ray2.30A1749-2209[»]
1VBDX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1XYRelectron microscopy11.001650-881[»]
297-333[»]
3391-572[»]
5342-353[»]
6355-390[»]
782-95[»]
8621-631[»]
2BBLNMR-A1544-1565[»]
2BBPNMR-A1544-1565[»]
2IJDX-ray3.401/21566-2208[»]
2IJFX-ray3.00A1749-2208[»]
2ILYX-ray2.60A1749-2208[»]
2ILZX-ray2.50A1749-2208[»]
2IM0X-ray2.25A1749-2208[»]
2IM1X-ray2.50A1749-2208[»]
2IM2X-ray2.35A1749-2208[»]
2IM3X-ray2.60A1749-2208[»]
2PLVX-ray2.881580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3EPCelectron microscopy8.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
3IYBelectron microscopy10.001647-881[»]
3342-572[»]
497-341[»]
3IYCelectron microscopy-1647-881[»]
497-341[»]
3J3Oelectron microscopy11.101580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3J3Pelectron microscopy9.101580-881[»]
270-341[»]
3342-579[»]
3J48electron microscopy5.501580-881[»]
270-341[»]
3342-579[»]
3J8Felectron microscopy3.701580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3J9Felectron microscopy9.001580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3JBCelectron microscopy5.601580-881[»]
270-341[»]
3342-578[»]
42-69[»]
3JBDelectron microscopy4.701580-881[»]
270-341[»]
3342-578[»]
42-69[»]
3JBEelectron microscopy4.201580-881[»]
270-341[»]
3342-578[»]
42-69[»]
3JBFelectron microscopy4.601580-881[»]
270-341[»]
3342-578[»]
42-69[»]
3JBGelectron microscopy3.801580-881[»]
270-341[»]
3342-578[»]
42-69[»]
3OL7X-ray2.70A/E/I/M1749-2209[»]
4DCDX-ray1.69A1566-1748[»]
4K4SX-ray2.40A/E1749-2209[»]
4K4TX-ray2.75A/E1749-2209[»]
4K4UX-ray2.85A/E1749-2209[»]
4K4VX-ray2.63A/E1749-2209[»]
4K4WX-ray2.69A/E1749-2209[»]
4NLOX-ray2.20A1749-2209[»]
4NLPX-ray2.20A1749-2209[»]
4NLQX-ray2.30A1749-2209[»]
4NLRX-ray2.00A1749-2209[»]
4NLSX-ray2.00A1749-2209[»]
4NLTX-ray2.50A1749-2209[»]
4NLUX-ray2.10A1749-2209[»]
4NLVX-ray2.30A1749-2209[»]
4NLWX-ray2.10A1749-2209[»]
4NLXX-ray2.60A1749-2209[»]
4NLYX-ray2.30A1749-2209[»]
4R0EX-ray3.00A1749-2209[»]
5KTZelectron microscopy4.301636-858[»]
270-338[»]
3342-572[»]
5KU0electron microscopy4.201636-858[»]
270-338[»]
3342-572[»]
5KU2electron microscopy4.501650-858[»]
270-337[»]
3342-571[»]
5KWLelectron microscopy4.501650-858[»]
270-337[»]
3342-571[»]
5Z3QX-ray2.54A/B/C/D/E/H1243-1456[»]
6HLVX-ray2.50B1457-1514[»]
SMRiP03300
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ELMiP03300
IntActiP03300, 4 interactors

Chemistry databases

BindingDBiP03300
ChEMBLiCHEMBL5127
DrugBankiDB08014 (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE
DB08012 (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE
DB08013 (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE
DB04137 Guanosine-5'-Triphosphate
DB08231 Myristic acid
DB03963 S-(Dimethylarsenic)Cysteine
DB03203 Sphingosine

Protein family/group databases

MEROPSiC03.001

PTM databases

iPTMnetiP03300

Proteomic databases

PRIDEiP03300

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P03300

Genome annotation databases

GeneIDi919920
KEGGivg:919920

Miscellaneous databases

EvolutionaryTraceiP03300

Family and domain databases

CDDicd00205 rhv_like, 3 hits
Gene3Di1.10.10.870, 1 hit
2.60.120.20, 3 hits
InterProiView protein in InterPro
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR014838 P3A
IPR036203 P3A_soluble_dom
IPR000081 Peptidase_C3
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR003138 Pico_P1A
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat
PfamiView protein in Pfam
PF08727 P3A, 1 hit
PF00548 Peptidase_C3, 1 hit
PF02226 Pico_P1A, 1 hit
PF00947 Pico_P2A, 1 hit
PF01552 Pico_P2B, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 3 hits
PF00910 RNA_helicase, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 1 hit
SSF89043 SSF89043, 1 hit
PROSITEiView protein in PROSITE
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_POL1M
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03300
Secondary accession number(s): P03299
, Q84879, Q84880, Q89679
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 13, 2019
This is version 211 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again